Q63716 (PRDX1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxiredoxin-1
EC=1.11.1.15

Alternative name(s):
HBP23
Heme-binding 23 kDa protein
Thioredoxin peroxidase 2
Thioredoxin-dependent peroxide reductase 2

Gene names

Name:	Prdx1
Synonyms:	Tdpx2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation By similarity.
Catalytic activity	2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.
Subunit structure	Homodimer; disulfide-linked, upon oxidation. May form heterodimers with AOP2. Interacts with GDPD5; forms a mixed-disulfide with GDPD5 By similarity.
Subcellular location	Cytoplasm. Melanosome By similarity.
Post-translational modification	Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity By similarity.
Miscellaneous	The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin. Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized.
Sequence similarities	Belongs to the AhpC/TSA family. Contains 1 thioredoxin domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Molecular function	Antioxidant Oxidoreductase Peroxidase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Inferred from electronic annotation. Source: Compara erythrocyte homeostasis Inferred from electronic annotation. Source: Compara hydrogen peroxide catabolic process Inferred from electronic annotation. Source: Compara natural killer cell mediated cytotoxicity Inferred from electronic annotation. Source: Compara regulation of NF-kappaB import into nucleus Inferred from electronic annotation. Source: Compara regulation of stress-activated MAPK cascade Inferred from electronic annotation. Source: Compara removal of superoxide radicals Inferred from electronic annotation. Source: Compara response to oxidative stress Inferred from direct assay PubMed 17556052. Source: RGD
Cellular_component	cytosol Inferred from direct assay PubMed 11350800PubMed 7488219Ref.1. Source: RGD melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial matrix Inferred from direct assay PubMed 14623930. Source: RGD nuclear euchromatin Inferred from direct assay PubMed 14623930. Source: RGD nucleolus Inferred from direct assay PubMed 14623930. Source: RGD peroxisomal matrix Inferred from direct assay PubMed 14623930. Source: RGD
Molecular_function	heme binding Inferred from physical interaction Ref.1. Source: RGD peroxiredoxin activity Inferred from direct assay PubMed 11350800PubMed 7488219. Source: RGD protein homodimerization activity Inferred from direct assay Ref.4. Source: RGD thioredoxin peroxidase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 199

198

Peroxiredoxin-1

PRO_0000135078

Regions

Domain

6 – 165

160

Thioredoxin

Sites

Active site

52

1

Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Modified residue

2

1

N-acetylserine By similarity

Modified residue

7

1

N6-acetyllysine By similarity

Modified residue

16

1

N6-acetyllysine By similarity

Modified residue

27

1

N6-acetyllysine By similarity

Modified residue

35

1

N6-acetyllysine By similarity

Modified residue

90

1

Phosphothreonine By similarity

Disulfide bond

52

Interchain (with C-173); in linked form

Disulfide bond

173

Interchain (with C-52); in linked form

Secondary structure

1

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199

Helix Strand Turn

Details...

Beta strand

16 – 20

5

Beta strand

26 – 30

5

Helix

31 – 34

4

Beta strand

37 – 43

7

Beta strand

50 – 52

3

Helix

57 – 61

5

Helix

63 – 68

6

Beta strand

71 – 78

8

Helix

81 – 88

8

Helix

92 – 94

3

Beta strand

104 – 106

3

Helix

111 – 115

5

Beta strand

121 – 124

4

Beta strand

128 – 133

6

Beta strand

137 – 145

9

Helix

153 – 168

16

Beta strand

170 – 172

3

Turn

188 – 191

4

Helix

192 – 195

4

Sequences

	Sequence		Length	Mass (Da)
	Q63716 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BDF2D4ABA8A776DA	FASTA	199	22,109
	10 20 30 40 50 60 MSSGNAKIGH PAPSFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS 70 80 90 100 110 120 DRAEEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK 130 140 150 160 170 180 ADEGISFRGL FIIDDKGILR QITINDLPVG RSVDEILRLV QAFQFTDKHG EVCPAGWKPG 190 SDTIKPDVNK SKEYFSKQK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification, characterization, and cloning of a heme-binding protein (23 kDa) in rat liver cytosol." Iwahara S., Satoh H., Song D.-X., Webb J., Burlingame A.L., Nagae Y., Mueller-Eberhard U. Biochemistry 34:13398-13406(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver and Pituitary.
[3]	Lubec G., Afjehi-Sadat L., Diao W., Kang S.U. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 17-35 AND 111-190, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain, Hippocampus and Spinal cord.
[4]	"Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product." Hirotsu S., Abe Y., Okada K., Nagahara N., Hori H., Nishino T., Hakoshima T. Proc. Natl. Acad. Sci. U.S.A. 96:12333-12338(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN OXIDIZED FORM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D30035 mRNA. Translation: BAA06275.1.
BC058450 mRNA. Translation: AAH58450.1.
BC088118 mRNA. Translation: AAH88118.1.

IPI

IPI00211779.

PIR

I52425.

RefSeq

NP_476455.1. NM_057114.1.

UniGene

Rn.2845.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QQ2	X-ray	2.60	A/B	1-199	[»]
2Z9S	X-ray	2.90	A/B/C/D/E/F/G/H/I/J	1-199	[»]

ProteinModelPortal

Q63716.

SMR

Q63716. Positions 3-199.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q63716. 3 interactions.

STRING

10116.ENSRNOP00000023132.

Protein family/group databases

PeroxiBase

4508. Rno2CysPrx01.

PTM databases

PhosphoSite

Q63716.

2D gel databases

World-2DPAGE

0004:Q63716.

Proteomic databases

PaxDb

Q63716.

PRIDE

Q63716.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000023132; ENSRNOP00000023132; ENSRNOG00000017194.

GeneID

117254.

KEGG

rno:117254.

UCSC

RGD:620039. rat.

Organism-specific databases

CTD

5052.

RGD

620039. Prdx1.

Phylogenomic databases

eggNOG

COG0450.

GeneTree

ENSGT00390000004653.

HOGENOM

HOG000022343.

HOVERGEN

HBG000286.

InParanoid

Q63716.

KO

K13279.

OMA

TISTDYG.

OrthoDB

EOG4V6ZHJ.

Gene expression databases

Genevestigator

Q63716.

GermOnline

ENSRNOG00000017194. Rattus norvegicus.

Family and domain databases

Gene3D

3.40.30.10. 1 hit.

InterPro

IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]

PIRSF

PIRSF000239. AHPC. 1 hit.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q63716.

NextBio

620108.

Entry information

Entry name

PRDX1_RAT

Accession

Primary (citable) accession number: Q63716

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program